ID A0A0V1I3C2_9BILA Unreviewed; 724 AA.
AC A0A0V1I3C2;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 22-FEB-2023, entry version 22.
DE SubName: Full=Beta-amyloid-like protein {ECO:0000313|EMBL:KRZ17279.1};
DE Flags: Fragment;
GN Name=apl-1 {ECO:0000313|EMBL:KRZ17279.1};
GN ORFNames=T11_1408 {ECO:0000313|EMBL:KRZ17279.1};
OS Trichinella zimbabwensis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=268475 {ECO:0000313|EMBL:KRZ17279.1, ECO:0000313|Proteomes:UP000055024};
RN [1] {ECO:0000313|EMBL:KRZ17279.1, ECO:0000313|Proteomes:UP000055024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS1029 {ECO:0000313|EMBL:KRZ17279.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC -!- SIMILARITY: Belongs to the APP family. {ECO:0000256|PROSITE-
CC ProRule:PRU01217}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01217}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRZ17279.1}.
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DR EMBL; JYDP01000007; KRZ17279.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1I3C2; -.
DR STRING; 268475.A0A0V1I3C2; -.
DR Proteomes; UP000055024; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046914; F:transition metal ion binding; IEA:InterPro.
DR Gene3D; 1.20.120.770; Amyloid precursor protein, E2 domain; 1.
DR Gene3D; 3.30.1490.140; Amyloidogenic glycoprotein, copper-binding domain; 1.
DR Gene3D; 3.90.570.10; Amyloidogenic glycoprotein, heparin-binding domain; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR036669; Amyloid_Cu-bd_sf.
DR InterPro; IPR008155; Amyloid_glyco.
DR InterPro; IPR011178; Amyloid_glyco_Cu-bd.
DR InterPro; IPR024329; Amyloid_glyco_E2_domain.
DR InterPro; IPR008154; Amyloid_glyco_extra.
DR InterPro; IPR015849; Amyloid_glyco_heparin-bd.
DR InterPro; IPR036454; Amyloid_glyco_heparin-bd_sf.
DR InterPro; IPR019543; APP_amyloid_C.
DR InterPro; IPR019744; APP_CUBD_CS.
DR InterPro; IPR036176; E2_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR PANTHER; PTHR23103; ALZHEIMER'S DISEASE BETA-AMYLOID RELATED; 1.
DR PANTHER; PTHR23103:SF15; AMYLOID-BETA-LIKE PROTEIN; 1.
DR Pfam; PF10515; APP_amyloid; 1.
DR Pfam; PF12924; APP_Cu_bd; 1.
DR Pfam; PF12925; APP_E2; 1.
DR Pfam; PF02177; APP_N; 1.
DR PRINTS; PR00203; AMYLOIDA4.
DR SMART; SM00006; A4_EXTRA; 1.
DR SUPFAM; SSF56491; A heparin-binding domain; 1.
DR SUPFAM; SSF89811; Amyloid beta a4 protein copper binding domain (domain 2); 1.
DR SUPFAM; SSF109843; CAPPD, an extracellular domain of amyloid beta A4 protein; 1.
DR PROSITE; PS00319; APP_CUBD; 1.
DR PROSITE; PS51869; APP_E1; 1.
DR PROSITE; PS51870; APP_E2; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU01217}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000055024};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..39
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 659..679
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 64..224
FT /note="E1"
FT /evidence="ECO:0000259|PROSITE:PS51869"
FT DOMAIN 330..529
FT /note="E2"
FT /evidence="ECO:0000259|PROSITE:PS51870"
FT REGION 64..157
FT /note="GFLD subdomain"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT REGION 165..224
FT /note="CuBD subdomain"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT REGION 245..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 362..422
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 263..286
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..326
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 74..97
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT DISULFID 133..140
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRZ17279.1"
SQ SEQUENCE 724 AA; 83239 MW; 08453538000D4FC2 CRC64;
LCHASRSLSS LVRWLMVKML LNLAFFVLSI CLNFAVGSIE LTRLQAVSGG YAGSAASNHK
TKANAFVPQV VFHCGFRNRY MTEDGSWASD PDSRASCLTG KLDILKYCRK VYWNLTVTNI
VESSHFVEVD NWCKDDGYPC KWSFWVKPYR CMVGEFESDA LLVPKNCHFE HVDDENICKD
FDYWNQTAIK NCKRRNSYSV LSFAMLEPCG LDMFSGVEFV CCPNRDDINA NVVNVGRLSI
RMQSSRDREN ELYGPAIPND SEEYPPTVTT TTTATRTHST VPPPALLTTA SPKAATDDED
EDDDEDYEEE DDDDDDDDDA ENEDADTDNE KSVYLRVADP EIEHEAYKNA LEHLTKVHHK
KVSKVMKEWS ELENRYQEMK RRDPKHAESF KNEMNMRFQK TVAALEEENA DERHQIEDIH
QQRVMANLNE KKRLALKEFH QLYDVAGPPP AHAILRTLKA YVRAEEKDRV HLLNHYRHML
RSKPQESIFF KSDVLNKLLD IDRRINATIS LLKLHPEIDK KVRAAIEDFF YTYRRENTPD
IAETFPDGYL NSAQYHQLLN MYQARIIGNN NAYGRKMTVD QIITLAPSVK VQQRKEITEN
TIDAVQRQEQ TISTLPLRNI HVVEEDISLL NKKQDIVHDF VFQEKSIGKG ASKYIDHSFI
FFSIAGVSLI AAVVCGIFFM RHRANHAGQG FIEVSACTPE ERHVANMQIS GYENPAYKYF
EENL
//
